ArticleBiochemistry2011
Chlamydia protease-like activity factor (CPAF): characterization of proteolysis activity in vitro and development of a nanomolar affinity CPAF zymogen-derived inhibitor.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Review
- Insights into the Autoproteolytic Processing and Catalytic Mechanism of theBiochemistry · 2019Article
- Chlamydia trachomatis paralyses neutrophils to evade the host innate immune response.Nature microbiology · 2018Article
- Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton.eLife · 2018Article
- Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics.Molecular & cellular proteomics : MCP · 2016Article
- Article
- SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors.Molecular biology of the cell · 2015Article
- Article
- Analysis of CPAF mutants: new functions, new questions (the ins and outs of a chlamydial protease).Pathogens and disease · 2014Article
- Reassessing the role of the secreted protease CPAF in Chlamydia trachomatis infection through genetic approaches.Pathogens and disease · 2014Article
- Chlamydia trachomatis outer membrane complex protein B (OmcB) is processed by the protease CPAF.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
During infection of epithelial cells, the obligate intracellular pathogen Chlamydia trachomatis secretes the serine protease Chlamydia protease-like activity factor (CPAF) into the host cytosol to regulate a range of host cellular processes through targeted proteolysis. Here we report the development of an in vitro assay for the enzyme and the discovery of a cell-permeable CPAF zymogen-based peptide inhibitor with nanomolar inhibitory affinity. Treating C. trachomatis-infected HeLa cells with this inhibitor prevented CPAF cleavage of the intermediate filament vimentin and led to the loss of vimentin cage surrounding the intracellular vacuole. Because Chlamydia is a genetically intractable organism, this inhibitor may serve as a tool for understanding the role of CPAF in pathogenesis.
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Registered trials
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